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We report on the measurement of the beam asymmetry ς for the reactions γ - p→pη and γ - p→pη′ from the GlueX experiment using an 8.2-8.8-GeV linearly polarized tagged photon beam incident on a liquid hydrogen target in Hall D at Jefferson Laboratory. These measurements are made as a function of momentum transfer -t with significantly higher statistical precision than our earlier η measurements and are the first measurements of η′ in this energy range. We compare the results to theoretical predictions based on t-channel quasiparticle exchange. We also compare the ratio of ςη to ςη′ to these models as this ratio is predicted to be sensitive to the amount of ss exchange in the production. We find that photoproduction of both η and η′ is dominated by natural parity exchange with little dependence on -t. © 2019 American Physical Society.

The barrel calorimeter is part of the new spectrometer installed in Hall D at Jefferson Lab for the GlueX experiment. The calorimeter was installed in 2013, commissioned in 2014 and has been operating routinely since early 2015. The detector configuration, associated Monte Carlo simulations, calibration and operational performance are described herein. The calorimeter records the time and energy deposited by charged and neutral particles created by a multi-GeV photon beam. It is constructed as a lead and scintillating-fiber calorimeter and read out with 3840 large-area silicon photomultiplier arrays. Particles impinge on the detector over a wide range of angles, from normal incidence at 90 degrees down to 11.5 degrees, which defines a geometry that is fairly unique among calorimeters. The response of the calorimeter has been measured during a running experiment and performs as expected for electromagnetic showers below 2.5 GeV. We characterize the performance of the BCAL using the energy resolution integrated over typical angular distributions for π0 and η production of σE∕E=5.2%∕E(GeV)⊕3.6% and a timing resolution of σ=150 ps at 1 GeV. © 2018

We report measurements of the photon beam asymmetry Σ for the reactions γ - p→pπ0 and γ - p→pη from the GlueX experiment using a 9 GeV linearly polarized, tagged photon beam incident on a liquid hydrogen target in Jefferson Lab's Hall D. The asymmetries, measured as a function of the proton momentum transfer, possess greater precision than previous π0 measurements and are the first η measurements in this energy regime. The results are compared with theoretical predictions based on t-channel, quasiparticle exchange and constrain the axial-vector component of the neutral meson production mechanism in these models. © 2017 American Physical Society.

Results on two-particle correlations, deuteron production, event anisotropy and event-by-event fluctuations of 〈pT〉 and K/π were obtained by the NA49 experiment in Pb+Pb collisions at 158 A·GeV beam energy. The interpretation of the measurements is discussed in light of the search for deconfinement. © 2001 Elsevier Science B.V. All rights reserved.

New data with a minimum bias trigger for 158 GeV/nucleon Pb + Pb have been analyzed. Directed and elliptic flow as a function of rapidity of the particles and centrality of the collision are presented. The centrality dependence of the ratio of elliptic flow to the initial space elliptic anisotropy is compared to models.

Strangeness measurements in NA49 indicate a strangeness enhancement in Pb + Pb interactions, relative to the elementary nucleon-nucleon and nucleon-nucleus collisions. It appears that the magnitude of the enhancement is similar in Pb + Pb and S + nucleus collisions. The enhancement is present in almost every central Pb + Pb collision, the dynamical fluctuations (in strangeness) appear to be minimal. The magnitude of the enhancement increases with the strangeness content of the particle species. The inverse slope systematics indicate the presence of transverse flow in the system. The cascade/lambda ratio is increased relative to elementary collisions.

In memory of the 85th birthday of Yakov S. Lebedev (Moscow), who died in 1996, we start this Review on soft-glass matrix effects in donor–acceptor complexes with an appreciation of his pioneering work on high-field EPR spectroscopy on tribochemically generated donor–acceptor complexes. The mechanochemical activation of polycrystalline mixtures of porphyrins (and other donors) and quinone acceptors was found to produce large concentrations of triplet donor molecules and donor–acceptor radical pairs with unusual stability. The Review is continued with reporting on W-band high-field EPR and fast-laser studies on disaccharide matrix effects on structure and dynamics of donor–acceptor protein complexes related to photosynthesis, including the non-oxygenic bacterial reaction center (RC) and the oxygenic RCs Photosystem I (PS I) and Photosystem II (PS II, preliminary results). Some organisms can survive complete dehydration and high temperatures by adopting an anhydrobiotic state in which the intracellular medium contains large amounts of disaccharides, in particular trehalose and sucrose. Trehalose is most effective in protecting biostructures, both in vivo and in vitro. To clarify the molecular mechanisms of disaccharide bioprotection, structure and dynamics of sucrose and trehalose matrices at different controlled hydration levels were probed by perdeuterated nitroxide spin labels and native cofactor intermediates in their charge-separated states. Trehalose forms a homogeneous amorphous phase in which the hosted molecules are uniformly distributed. Notably, their rotational mobility at room temperature is dramatically impaired by thetrehalose H-bonding network confinement to an extent that in normal protein–matrix systems is only observed at low temperatures around 150K. From the experimental results, formation of an extended H-bonding network of trehalose with protein molecules is inferred, involving both bulk and local water molecules. The H-bond network extends homogeneously over the whole matrix integrating and immobilizing the hosted protein. Taken together, these observations suggest that in photosystems, such as bacterial RCs and PS I complexes, of different size and complexity regarding subunit composition and oligomeric organization, the molecular configuration of the cofactors involved in the primary processes of charge separation is not significantly distorted by incorporation into trehalose glass, even under extensive dehydration. By means of pulsed W-band high-field multiresonance EPR spectroscopies, such as ELDOR-detected NMR and ENDOR, in conjunction with using isotope labeled water (D2O and H217O), the biologically important issue of sensing and quantification of local water in proteins is addressed. The bacterial RC embedded into the trehalose glass matrix is used as model system. The two native radical cofactor ions of the primary electron donor and acceptor as well as an artificial nitroxide spin label site-specifically attached to the protein surface are studied in the experiments. The three paramagnetic reporter groups probe distinctly different local environments. They sense water molecules via their magnetic hyperfine and quadrupole interactions with either deuterons or 17O nuclei. It is shown that by using oxygen-17 labeled water, quantitative conclusions can be drawn differentiating between local and bulk water. It is concluded that dry trehalose operates as anhydrobiotic protein stabilizer by means of selective changes in the first solvation shell of the protein upon trehalose–matrix dehydration with subsequent changes in the hydrogen-bonding network. Such changes usually have an impact on the global function of a biological system. Finally, preliminary results of optical and W-band EPR experiments on the extremolytes ectoine and its derivative hydroxyectoine are reported; these compounds appear to share several stress-protecting properties with trehalose in terms of stabilizing protein matrices. For instance, they display remarkable stabilizing capabilities towards sensitive proteins and enzymes with respect to freeze-thawing, heat-treatment, and freeze-drying procedures. Moreover, hydroxyectoine is a good glass-forming compound and exhibits a remarkable bioprotective effect against desiccation and heat denaturation of functional protein complexes.

In the present study, we have investigated the effect of hydroxyectoine (Ect-OH), a heterocyclic amino acid, on oxygen evolution in photosystem II (PS II) membrane fragments and on photoinhibition of Mn-depleted PS II (apo-WOC-PS II) preparations. The degree of photoinhibition of apo-WOC-PS II preparations was estimated by the loss of the capability of exogenous electron donor (sodium ascorbate) to restore the amplitude of light-induced changes of chlorophyll fluorescence yield (∆F). It was found that Ect-OH (i) stimulates the oxygen-evolving activity of PS II, (ii) accelerates the electron transfer from exogenous electron donors (K4[Fe(CN)6], DPC, TMPD, Fe2+, and Mn2+) to the reaction center of apo-WOC-PS II, (iii) enhances the protective effect of exogenous electron donors against donor-side photoinhibition of apo-WOC-PS II preparations. It is assumed that Ect-OH can serve as an artificial electron donor for apo-WOC-PS II, which does not directly interact with either the donor or acceptor side of the reaction center. We suggest that the protein conformation in the presence of Ect-OH, which affects the extent of hydration, becomes favorable for accepting electrons from exogenous donors. To our knowledge, this is the first study dealing with redox activity of Ect-OH towards photosynthetic pigment–protein complexes.

The kinetics of electron transfer from reduced high-potential iron-sulfur protein (HiPIP) to the photooxidized tetraheme cytochrome c subunit (THC) bound to the photosynthetic reaction center (RC) from the purple sulfur bacterium Allochromatium vinosum were studied under controlled redox conditions by flash absorption spectroscopy. At ambient redox potential Eh = +200 mV, where only the high-potential (HP) hemes of the THC are reduced, the electron transfer from HiPIP to photooxidized HP heme(s) follows second-order kinetics with rate constant k = (4.2 +/- 0.2) 10(5) M(-1) s(-1) at low ionic strength. Upon increasing the ionic strength, k increases by a maximum factor of ca. 2 at 640 mM KCl. The role of Phe48, which lies on the external surface of HiPIP close to the [Fe4S4] cluster and presumably on the electron transfer pathway to cytochrome heme(s), was investigated by site-directed mutagenesis. Substitution of Phe48 with arginine, aspartate, and histidine completely prevents electron donation. Conversely, electron transfer is still observed upon substitution of Phe48 with tyrosine and tryptophan, although the rate is decreased by more than 1 order of magnitude. These results suggest that Phe48 is located on a key protein surface patch essential for efficient electron transfer, and that the presence of an aromatic hydrophobic residue on the putative electron-transfer pathway plays a critical role. This conclusion was supported by protein docking calculations, resulting in a structural model for the HiPIP-THC complex, which involves a docking site close to the LP heme farthest from the bacteriochlorophyll special pair.